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| - | [[Image:1t5d.gif|left|200px]] | |
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| - | {{Structure
| + | ==4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate== |
| - | |PDB= 1t5d |SIZE=350|CAPTION= <scene name='initialview01'>1t5d</scene>, resolution 2.206Å
| + | <StructureSection load='1t5d' size='340' side='right'caption='[[1t5d]], [[Resolution|resolution]] 2.21Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=174:4-CHLORO-BENZOIC+ACID'>174</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
| + | <table><tr><td colspan='2'>[[1t5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_sp._AL3007 Alcaligenes sp. AL3007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T5D FirstGlance]. <br> |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4-chlorobenzoate--CoA_ligase 4-chlorobenzoate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.33 6.2.1.33] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.206Å</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=174:4-CHLORO-BENZOIC+ACID'>174</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5d OCA], [https://pdbe.org/1t5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t5d RCSB], [https://www.ebi.ac.uk/pdbsum/1t5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t5d ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=[[1pg4|1PG4]], [[1ry2|1RY2]], [[1amu|1AMU]], [[1mdb|1MDB]]
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5d OCA], [http://www.ebi.ac.uk/pdbsum/1t5d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t5d RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/Q8GN86_9BURK Q8GN86_9BURK] |
| - | | + | == Evolutionary Conservation == |
| - | '''4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t5/1t5d_consurf.spt"</scriptWhenChecked> |
| - | 4-Chlorobenzoate:CoA ligase (CBAL) is a member of a family of adenylate-forming enzymes that catalyze two-step adenylation and thioester-forming reactions. In previous studies, we have provided structural evidence that members of this enzyme family (exemplified by acetyl-CoA synthetase) use a large domain rotation to catalyze the respective partial reactions [A. M. Gulick, V. J. Starai, A. R. Horswill, K. M. Homick, and J. C. Escalante-Semerena, (2003) Biochemistry 42, 2866-2873]. CBAL catalyzes the synthesis of 4-chlorobenzoyl-CoA, the first step in the 4-chlorobenzoate degredation pathway in PCB-degrading bacteria. We have solved the 2.0 A crystal structure of the CBAL enzyme from Alcaligenes sp. AL3007 using multiwavelength anomalous dispersion. The results demonstrate that in the absence of any ligands, or bound to the aryl substrate 4-chlorobenzoate, the enzyme adopts the conformation poised for catalysis of the adenylate-forming half-reaction. We hypothesize that coenzyme A binding is required for stabilization of the alternate conformation, which catalyzes the 4-CBA-CoA thioester-forming reaction. We have also determined the structure of the enzyme bound to the aryl substrate 4-chlorobenzoate. The aryl binding pocket is composed of Phe184, His207, Val208, Val209, Phe249, Ala280, Ile303, Gly305, Met310, and Asn311. The structure of the 4-chlorobenzoate binding site is discussed in the context of the binding sites of other family members to gain insight into substrate specificity and evolution of new function.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1T5D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp._al3007 Alcaligenes sp. al3007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5D OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t5d ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference==
| + | __TOC__ |
| - | Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states., Gulick AM, Lu X, Dunaway-Mariano D, Biochemistry. 2004 Jul 13;43(27):8670-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15236575 15236575]
| + | </StructureSection> |
| - | [[Category: 4-chlorobenzoate--CoA ligase]]
| + | [[Category: Alcaligenes sp. AL3007]] |
| - | [[Category: Alcaligenes sp. al3007]] | + | [[Category: Large Structures]] |
| - | [[Category: Single protein]] | + | [[Category: Dunaway-Mariano D]] |
| - | [[Category: Dunaway-Mariano, D.]] | + | [[Category: Gulick AM]] |
| - | [[Category: Gulick, A M.]] | + | [[Category: Lu X]] |
| - | [[Category: Lu, X.]] | + | |
| - | [[Category: adenylate-forming]]
| + | |
| - | [[Category: coenzyme some]]
| + | |
| - | [[Category: conformational change]]
| + | |
| - | [[Category: domain alternation]]
| + | |
| - | [[Category: ligase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:51:32 2008''
| + | |
